ArticleNanoscale2022
Single molecule iSCAT imaging reveals a fast, energy efficient search mode for the DNA repair protein UvrA.
Article in Nanoscale, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structural snapshots of the mechanism of ATP-dependent DNA damage recognition by UvrA.Nature communications · 2025Article
- Mechanistic understanding of UvrA damage detection and lesion hand-off to UvrB in Nucleotide Excision Repair.Nature communications · 2025Article
- Identification of a novel DNA repair inhibitor using an in silico driven approach shows effective combinatorial activity with genotoxic agents against multidrug-resistant Escherichia coli.Protein science : a publication of the Protein Society · 2024Article
- Developing novel antimicrobials by combining cancer chemotherapeutics with bacterial DNA repair inhibitors.PLoS pathogens · 2023Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Exposure to UV radiation results in numerous DNA lesions, which threaten genome integrity. The nucleotide excision DNA repair pathway detects and repairs a range of such UV-induced DNA lesions. In bacteria, initial damage detection and verification is carried out by two proteins: UvrA and UvrB. Despite decades of study, the process of how these proteins locate damage remains unclear. Here we use high-speed interferometric scattering (iSCAT) microscopy, in combination with a surface-bound-DNA assay, to investigate early damage detection by UvrA. We have discovered that UvrA interacts with DNA in two phases; a slow phase (∼1.3 s
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